Evaluation of the Binding Properties of A New Phenylurea Appended Carbazole Compound to Pepsin/Trypsin by Computational and Multi-Spectral Analysis

被引：2

作者：

Gokoglu, Elmas ^{[1
]}

Doyuran, Bensu ^{[1
]}

Ozen, Guelsah ^{[1
]}

Duyar, Halil ^{[2
]}

Taskin-Tok, Tugba ^{[3
,4
]}

Seferoglu, Zeynel ^{[5
]}

机构：

[1] Hacettepe Univ, Dept Chem, TR-06800 Ankara, Turkiye

[2] Gebze Tech Univ, Dept Chem, TR-41400 Kocaeli, Turkiye

[3] Gaziantep Univ, Dept Chem, TR-27310 Gaziantep, Turkiye

[4] Gaziantep Univ, Dept Bioinformat & Computat Biol, TR-27310 Gaziantep, Turkiye

[5] Gazi Univ, Dept Chem, TR-06500 Ankara, Turkiye

来源：

JOURNAL OF FLUORESCENCE | 2024年 / 34卷 / 05期

关键词：

Carbazole; Protease; Thermodynamic parameter; Molecular docking. FRET; HUMAN SERUM-ALBUMIN; SPECTROSCOPIC ANALYSIS; DNA; DERIVATIVES; DESIGN; ACID;

D O I：

10.1007/s10895-023-03451-5

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

A novel carbazole compound, named 1-(9-ethyl-9H-carbazol-3-yl)-3-phenylurea (Cpu) was synthesized and its binding properties with protease enzymes (pepsin and trypsin) has been examined by steady-state fluorescence measurements, UV/vis absorption, infrared (FT-IR) and circular dicroism (CD) spectroscopies and also computational methods. The fluorescence experimental results indicated that the quenching mechanism of enzyme by Cpu is static process. The thermodynamic parameters (both negative Delta H/Delta S) and molecular docking results suggested that the binding of Cpu to pepsin/trypsin were driven by hydrogen bonds and van der Waals forces. Based on Forster's theory, the binding distance (r) between pepsin/trypsin and Cpu was calculated to be 3.072/2.784 nm, which implies that non-radiative energy transfer occurs from enzyme to Cpu. Furthermore, absorption, CD, and FT-IR spectral analysis provided an evidence that the presence of Cpu induced notable changes in the secondary structures and microenvironmental of both pepsin and trypsin, supporting its significant influence on these enzymes.

引用

页码：2359 / 2371

页数：13